SUV39H1

Supresor homólogo 1 de la variegación 3-9 homólogo 1 (Drosophila)
Estructuras disponibles
PDB	Buscar ortólogos: PDBe, RCSB Lista de códigos PDB 3MTS Estructuras enzimáticas RCSB PDB, PDBe, PDBsum
Identificadores
Símbolos	SUV39H1 (HGNC: 11479) ; H3-K9-HMTase 1; KMT1A; MG44; SUV39H
Identificadores; externos	OMIM: 300254 ; MGI: 1099440 ; HomoloGene: 2388 ; ChEMBL: 1795118; EBI: SUV39H1; GeneCards: Gen SUV39H1; UniProt: SUV39H1; Bases de datos de enzimas IntEnz: entrada en IntEnz; BRENDA: entrada en BRENDA; ExPASy: NiceZime view; KEGG: entrada en KEEG; PRIAM: perfil PRIAM; ExplorEnz: entrada en ExplorEnz; MetaCyc: vía metabólica
Número EC	2.1.1.43
Función molecular	• transcription regulatory region sequence-specific DNA binding; • chromatin binding; • protein binding; • zinc ion binding; • S-adenosylmethionine-dependent methyltransferase activity; • histone-lysine N-methyltransferase activity; • histone methyltransferase activity; • histone methyltransferase activity (H3-K9 specific); • protein N-terminus binding;
Componente celular	• chromosome, centromeric region; • heterochromatin; • condensed nuclear chromosome; • nucleus; • nuclear lamina; • nucleoplasm; • chromatin silencing complex; • rDNA heterochromatin;
Proceso biológico	• chromatin silencing at rDNA; • chromatin organization; • transcription, DNA-templated; • rRNA processing; • cell cycle; • viral process; • cell differentiation; • histone H3-K9 dimethylation; • histone H3-K9 trimethylation; • negative regulation of circadian rhythm; • negative regulation of transcription, DNA-templated; • rhythmic process;
	Referencias: AmiGO / QuickGO
Patrón de expresión de ARNm
	Más información
Ortólogos
Humano	Ratón
6839	20937
Véase HS	Véase MM
O43463	O54864
NM_001282166	NM_001290716
NP_001269095	NP_001277645
Cr. HG1436_HG1432_PATCH:; 48.55 – 48.57 Mb	Cr. X:; 8.06 – 8.07 Mb
[1] ;	[2]
	v; t; e;
	[editar datos en Wikidata]

La histona-lisina N-metiltransferasa (SUV39H1) es una enzima codificada en humanos por el gen suv39H1.^[1]

Esta proteína pertenece a la familia de supresores homólogos de la variegación 3-9 y posee un cromodominio y un dominio SET C-terminal. Esta proteína nuclear se dirige a los centrómeros durante la mitosis y funciona como una histona metiltransferasa, metilando la lisina 9 de la histona H3. Además, juega un papel crucial en la organización de la heterocromatina, en la segregación de los cromosomas durante la anafase y en la correcta progresión de la mitosis.^[2]

Interacciones

La enzima SUV39H1 ha demostrado ser capaz de interaccionar con:

Referencias

↑ ^a ^b Aagaard, L; Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh P B, Reuter G, Jenuwein T (Apr. de 1999). «Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31». EMBO J. (Inglaterra) 18 (7): 1923-38. ISSN 0261-4189. PMID 10202156. doi:10.1093/emboj/18.7.1923.
↑ «Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)».
↑ ^a ^b ^c Vaute, Olivier; Nicolas Estelle, Vandel Laurence, Trouche Didier (Jan. de 2002). «Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases». Nucleic Acids Res. (Inglaterra) 30 (2): 475-81. PMID 11788710.
↑ ^a ^b Zhang, Chun Li; McKinsey Timothy A, Olson Eric N (Oct. de 2002). «Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation». Mol. Cell. Biol. (EE. UU.) 22 (20): 7302-12. ISSN 0270-7306. PMID 12242305.
↑ Nielsen, S J; Schneider R, Bauer U M, Bannister A J, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera R E, Kouzarides T (Aug. de 2001). «Rb targets histone H3 methylation and HP1 to promoters». Nature (Inglaterra) 412 (6846): 561-5. ISSN 0028-0836. PMID 11484034. doi:10.1038/35087620.
↑ Vandel, L; Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D (Oct. de 2001). «Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase». Mol. Cell. Biol. (EE. UU.) 21 (19): 6484-94. ISSN 0270-7306. PMID 11533237.
↑ ^a ^b Fujita, Naoyuki; Watanabe Sugiko, Ichimura Takaya, Tsuruzoe Shu, Shinkai Yoichi, Tachibana Makoto, Chiba Tsutomu, Nakao Mitsuyoshi (Jun. de 2003). «Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression». J. Biol. Chem. (EE. UU.) 278 (26): 24132-8. ISSN 0021-9258. PMID 12711603. doi:10.1074/jbc.M302283200.
↑ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. de 2005). «Towards a proteome-scale map of the human protein-protein interaction network». Nature (Inglaterra) 437 (7062): 1173-8. PMID 16189514. doi:10.1038/nature04209.
↑ Fuks, François; Hurd Paul J, Deplus Rachel, Kouzarides Tony (mayo. de 2003). «The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase». Nucleic Acids Res. (Inglaterra) 31 (9): 2305-12. PMID 12711675.
↑ Chakraborty, Soumen; Sinha Kislay Kumar, Senyuk Vitalyi, Nucifora Giuseppina (Aug. de 2003). «SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo». Oncogene (Inglaterra) 22 (34): 5229-37. ISSN 0950-9232. PMID 12917624. doi:10.1038/sj.onc.1206600.
↑ Firestein, R; Cui X, Huie P, Cleary M L (Jul. de 2000). «Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9». Mol. Cell. Biol. (EE. UU.) 20 (13): 4900-9. ISSN 0270-7306. PMID 10848615.

Datos: Q18031798

[pmid10202156-1] Aagaard, L; Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh P B, Reuter G, Jenuwein T (Apr. de 1999). «Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31». EMBO J. (Inglaterra) 18 (7): 1923-38. ISSN 0261-4189. PMID 10202156. doi:10.1093/emboj/18.7.1923.

[entrez-2] «Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)».

[pmid11788710-3] Vaute, Olivier; Nicolas Estelle, Vandel Laurence, Trouche Didier (Jan. de 2002). «Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases». Nucleic Acids Res. (Inglaterra) 30 (2): 475-81. PMID 11788710.

[pmid12242305-4] Zhang, Chun Li; McKinsey Timothy A, Olson Eric N (Oct. de 2002). «Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation». Mol. Cell. Biol. (EE. UU.) 22 (20): 7302-12. ISSN 0270-7306. PMID 12242305.

[pmid11484059-5] Nielsen, S J; Schneider R, Bauer U M, Bannister A J, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera R E, Kouzarides T (Aug. de 2001). «Rb targets histone H3 methylation and HP1 to promoters». Nature (Inglaterra) 412 (6846): 561-5. ISSN 0028-0836. PMID 11484034. doi:10.1038/35087620.

[pmid11533237-6] Vandel, L; Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D (Oct. de 2001). «Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase». Mol. Cell. Biol. (EE. UU.) 21 (19): 6484-94. ISSN 0270-7306. PMID 11533237.

[pmid12711603-7] Fujita, Naoyuki; Watanabe Sugiko, Ichimura Takaya, Tsuruzoe Shu, Shinkai Yoichi, Tachibana Makoto, Chiba Tsutomu, Nakao Mitsuyoshi (Jun. de 2003). «Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression». J. Biol. Chem. (EE. UU.) 278 (26): 24132-8. ISSN 0021-9258. PMID 12711603. doi:10.1074/jbc.M302283200.

[pmid16189514-8] Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. de 2005). «Towards a proteome-scale map of the human protein-protein interaction network». Nature (Inglaterra) 437 (7062): 1173-8. PMID 16189514. doi:10.1038/nature04209.

[pmid12711675-9] Fuks, François; Hurd Paul J, Deplus Rachel, Kouzarides Tony (mayo. de 2003). «The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase». Nucleic Acids Res. (Inglaterra) 31 (9): 2305-12. PMID 12711675.

[pmid12917624-10] Chakraborty, Soumen; Sinha Kislay Kumar, Senyuk Vitalyi, Nucifora Giuseppina (Aug. de 2003). «SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo». Oncogene (Inglaterra) 22 (34): 5229-37. ISSN 0950-9232. PMID 12917624. doi:10.1038/sj.onc.1206600.

[pmid10848615-11] Firestein, R; Cui X, Huie P, Cleary M L (Jul. de 2000). «Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9». Mol. Cell. Biol. (EE. UU.) 20 (13): 4900-9. ISSN 0270-7306. PMID 10848615.

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